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Journal of Bacteriology, May 1999, p. 3270-3276, Vol. 181, No. 10
Section of Molecular and Cellular Biology,
University of California, Davis, California 95616
Received 14 December 1998/Accepted 19 March 1999
The gene engE, coding for endoglucanase E, one of the
three major subunits of the Clostridium cellulovorans
cellulosome, has been isolated and sequenced. engE is
comprised of an open reading frame (ORF) of 3,090 bp and encodes a
protein of 1,030 amino acids with a molecular weight of 111,796. The
amino acid sequence derived from engE revealed a structure
consisting of catalytic and noncatalytic domains. The N-terminal-half
region of EngE consisted of a signal peptide of 31 amino acid residues
and three repeated surface layer homology (SLH) domains, which were
highly conserved and homologous to an S-layer protein from the
gram-negative bacterium Caulobacter crescentus. The
C-terminal-half region, which is necessary for the enzymatic function
of EngE and for binding of EngE to the scaffolding protein CbpA,
consisted of a catalytic domain homologous to that of family 5 of the
glycosyl hydrolases, a domain of unknown function, and a duplicated
sequence (DS or dockerin) at its C terminus. engE is
located downstream of an ORF, ORF1, that is homologous to the
Bacillus subtilis phosphomethylpyrimidine kinase (pmk) gene. The unique presence of three SLH domains and a
DS suggests that EngE is capable of binding both to CbpA to form a
CbpA-EngE cellulosome complex and to the surface layer of C. cellulovorans.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Three Surface Layer Homology Domains at the N
Terminus of the Clostridium cellulovorans Major Cellulosomal
Subunit EngE
*
Corresponding author. Mailing address: Section of
Molecular and Cellular Biology, University of California, Davis, CA
95616. Phone: (530) 752-3191. Fax: (530) 752-3085. E-mail:
rhdoi{at}ucdavis.edu.
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